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| | ==Solution structure of the prokaryotic Phospholipase A2 from Streptomyces violaceoruber== | | ==Solution structure of the prokaryotic Phospholipase A2 from Streptomyces violaceoruber== |
| - | <StructureSection load='1it4' size='340' side='right'caption='[[1it4]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1it4' size='340' side='right'caption='[[1it4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1it4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_violaceus-ruber"_(sic)_waksman_and_curtis_1916 "actinomyces violaceus-ruber" (sic) waksman and curtis 1916]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IT4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1it4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IT4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1it5|1it5]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1it4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1it4 OCA], [https://pdbe.org/1it4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1it4 RCSB], [https://www.ebi.ac.uk/pdbsum/1it4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1it4 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1it4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1it4 OCA], [https://pdbe.org/1it4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1it4 RCSB], [https://www.ebi.ac.uk/pdbsum/1it4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1it4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6UV28_STRVN Q6UV28_STRVN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Izuhara, M]] | + | [[Category: Streptomyces violaceoruber]] |
| - | [[Category: Koike, T]] | + | [[Category: Izuhara M]] |
| - | [[Category: Ohtani, K]] | + | [[Category: Koike T]] |
| - | [[Category: Sugiyama, M]] | + | [[Category: Ohtani K]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Sugiyama M]] |
| - | [[Category: Prokaryotic pla2]]
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| Structural highlights
Function
Q6UV28_STRVN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Until now, phospholipase A(2) (PLA(2); EC 3.1.14) has been found only from eukaryotic sources. In the present study, we found a secreted PLA(2), which is produced by a soil bacterium, Streptomyces violaceoruber A-2688, demonstrating that the enzyme is the first phospholipase A(2) identified in prokaryote. After characterization of the novel PLA(2), a gene encoding the enzyme was cloned, sequenced, and overexpressed using a Streptomyces host-vector system. The amino acid sequence showed that the prokaryotic PLA(2) has only four cysteines and less homology to the eukaryotic ones, which have 12-16 cysteines. The solution structures of the prokaryotic PLA(2), bound and unbound with calcium(II) ion, were determined by using the NMR technique and structure calculation. The overall structure of the S. violaceoruber PLA(2), which is composed of only five alpha-helices, is completely different from those of eukaryotic PLA(2)s, which consist of beta-sheets and alpha-helices. The structure of the calcium-binding domain is obviously distinct from that without the ion; the ligands for the calcium(II) ion are the two carboxylates of Asp(43) (monodentate) and Asp(65) (bidentate), the carbonyl oxygen of Leu(44), and three water molecules. A calcium-binding experiment showed that the calcium dissociation constant ( approximately 5 mm) for the prokaryotic PLA(2) is much larger than those of eukaryotic ones.
A novel prokaryotic phospholipase A2. Characterization, gene cloning, and solution structure.,Sugiyama M, Ohtani K, Izuhara M, Koike T, Suzuki K, Imamura S, Misaki H J Biol Chem. 2002 May 31;277(22):20051-8. Epub 2002 Mar 15. PMID:11897786[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sugiyama M, Ohtani K, Izuhara M, Koike T, Suzuki K, Imamura S, Misaki H. A novel prokaryotic phospholipase A2. Characterization, gene cloning, and solution structure. J Biol Chem. 2002 May 31;277(22):20051-8. Epub 2002 Mar 15. PMID:11897786 doi:http://dx.doi.org/10.1074/jbc.M200264200
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